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Literature summary extracted from

  • Mandal, A.; Liyanage, M.R.; Zaidi, A.; Johnson, C.K.
    Interchange of autoinhibitory domain conformations in plasma-membrane Ca2+-ATPase-calmodulin complexes (2008), Protein Sci., 17, 555-562.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.2.2.10 Calmodulin calmodulin stimulates Ca2+ pumping in the plasma-membrane Ca2+-ATPase by binding to an autoinhibitory domain, which then dissociates from the catalytic domain of PMCA to allow full activation of the enzyme. Although the purified PMCA exhibits a significant basal Ca2+-dependent ATPase activity, the addition of calmodulin fluorescently labeled with tetramethylrhodamine (120 nM) at a saturating Ca2+ concentration (0.1 mM) results in significant activation of PMCA. The enzyme is fully activated at 0.025 mM calmodulin. Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.10 plasma membrane
-
Homo sapiens 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.10 Ca2+ dependent on Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.10 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.2.2.10 calmodulin-Sepharose column chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.2.2.10 erythrocyte
-
Homo sapiens
-

Storage Stability

EC Number Storage Stability Organism
7.2.2.10 -80°C, 10 mM HEPES pH 7.4, no loss in activity Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.10 ATP + H2O + Ca2+/cis
-
Homo sapiens ADP + phosphate + Ca2+/trans
-
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Synonyms

EC Number Synonyms Comment Organism
7.2.2.10 plasma membrane Ca2+-ATPase
-
Homo sapiens
7.2.2.10 PMCA
-
Homo sapiens